Artículo

Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

Polyamines, when added to cell‐free protein‐synthesizing systems, have been shown either to reduce mistranslation or to increase it depending upon the composition of the reaction mixture. To study this question under conditions as natural as possible we investigated the effects of polyamines on the fidelity of protein synthesis in intact Escherichia coli bacterial cells, using strains which were auxotrophic for polyamine synthesis. Error was measured in two ways: (a) the incorporation of [3H]histidine into coat protein of bacteriophage MS2, the gene of which does not code for histidine, and (b) the synthesis of a basic variant of MS2 coat protein in which a lysine erroneously replaces an asparagine, causing a change in isoelectric point. We found that when cell cultures were supplemented with polyamines there was no effect on the first type of error and the second type decreased twofold. The measured errors occurred at the level of translation because their frequency increased in the presence of streptomycin and decreased in cells bearing a streptomycin‐resistance mutation known to lower the occurrence of translational misreading. The average erroneous incorporation per mol coat protein in the presence of polyamines was 1.43 ± 0.59 mmol histidine and 25–34 mmol lysine/asparagine substitution. The reason for the different effect of polyamines on the two types of error is not known but could be related to the difference between their corresponding frequencies or to codon‐specific effects. Copyright © 1986, Wiley Blackwell. All rights reserved

Registro:

Documento: Artículo
Título:Effect of polyamines on translation fidelity in vivo
Autor:McMURRY, L.M.; ALGRANATI, I.D.
Filiación:Instituto de Investigaciones Bioquimicas 'Fundación Campomar', Facultad de Ciencias Exactas y Naturales, Argentina
Consejo Nacional de Investigaciones Cientificas y Técnicas, Buenos Aires, Argentina
Palabras clave:carbon; diagnostic agent; histidine; leucine; MS2 coat protein; polyamine; tritium; virus protein; article; biosynthesis; codon; drug effect; isoelectric point; isolation and purification; metabolism; RNA translation; virus capsid; Capsid; Carbon Radioisotopes; Codon; Histidine; Isoelectric Point; Leucine; Polyamines; Support, Non-U.S. Gov't; Translation, Genetic; Tritium; Viral Proteins
Año:1986
Volumen:155
Número:2
Página de inicio:383
Página de fin:390
DOI: http://dx.doi.org/10.1111/j.1432-1033.1986.tb09502.x
Título revista:European Journal of Biochemistry
Título revista abreviado:Eur. J. Biochem.
ISSN:00142956
CAS:carbon, 7440-44-0; histidine, 645-35-2, 7006-35-1, 71-00-1; leucine, 61-90-5, 7005-03-0; tritium, 10028-17-8; Carbon Radioisotopes; Codon; Histidine, 71-00-1; Leucine, 61-90-5; MS2 coat protein; Polyamines; Tritium, 10028-17-8; Viral Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v155_n2_p383_McMURRY

Referencias:

  • Tabor, C.W., Tabor, H., (1976) Annu. Rev. Biochem., 45, pp. 285-306
  • (1981) Polyamines in biology and medicine, , Morris, D. R., Marton, L. J., eds, Dekker, New York
  • (1983) Advances in polyamine research, 4. , Bachrach, U., Kaye, A., Chayen, R., eds, Raven Press, New York
  • Algranati, I.D., Goldemberg, S.H., (1977) Trends Biochem. Sci., 2, pp. 272-274
  • Tabor, C.W., Tabor, H., (1984) Annu. Rev. Biochem., 53, pp. 749-790
  • Takeda, Y., (1969) J. Biochem. (Tokyo), 66, pp. 345-349
  • Takeda, Y., Igarashi, K., (1972) J. Bacteriol., 111, pp. 1-6
  • Igarashi, K., Sugawara, K., Izumi, I., Nagayama, C., Hirose, S., (1974) Eur. J. Biochem., 48, pp. 495-502
  • Atkins, J.F., Lewis, J.B., Anderson, C.W., Gesteland, R.F., (1975) J. Biol. Chem., 250, pp. 5688-5695
  • Thang, M.N., Dondon, L., Mohier, E., (1976) FEBS Lett., 61, pp. 85-90
  • Hunter, A.R., Farrell, P.J., Jackson, R.J., Hunt, T., (1977) Eur. J. Biochem., 75, pp. 149-157
  • Goldemberg, S.H., Algranati, I.D., (1981) Eur. J. Biochem., 111, pp. 251-255
  • Abraham, A.K., Olsnes, S., Pihl, A., (1979) FEBS Lett., 101, pp. 93-96
  • Igarashi, K., Kashiwagi, K., Aoki, R., Kojima, M., Hirose, S., (1979) Biochem. Biophys. Res. Commun., 91, pp. 440-448
  • Igarashi, K., Hashimoto, S., Miyake, A., Kashigawi, K., Hirose, S., (1982) J. Biochem. (Tokyo), 128, pp. 597-604
  • Jelenc, P.C., Kurland, C.G., (1979) Proc. Natl Acad. Sci. USA, 76, pp. 3174-3178
  • Thompson, R.C., Dix, D.B., Gerson, R.B., Karim, A.M., (1981) J. Biol. Chem., 256, pp. 6676-6681
  • Min Jou, W., Haegeman, G., Ysebaert, M., Fiers, W., (1972) Nature (Lond.), 237, pp. 82-88
  • Tabor, H., Tabor, C.W., Cohn, M.S., Hafner, E.W., (1981) J. Bacteriol., 147, pp. 702-704
  • Parker, J., Johnston, T.C., Borgia, P.T., Holtz, G., Remaut, E., Fiers, W., (1983) J. Biol. Chem., 258, pp. 10007-10012
  • Miller, J.H., (1972) Experiments in molecular genetics, , Cold Spring Harbor Laboratory, C. S. H., New York
  • Curtiss, R., III, (1981) Manual of methods for general bacteriology, pp. 243-265. , Gerhardt, P., American Society for Microbiology, Washington, DC
  • Bjare, U., Gorini, L., (1971) J. Mol. Biol., 57, pp. 423-435
  • Goldemberg, S.H., Algranati, I.D., (1977) Mol. Cell. Biochem., 16, pp. 71-77
  • Hafner, E.W., Tabor, C.W., Tabor, H., (1979) J. Biol Chem., 254, pp. 12419-12426
  • Low, K.B., (1972) Bacteriol. Rev., 36, pp. 587-607
  • Zinder, N.D., (1975) RNA phages, , Cold Spring Harbor Laboratory, C. S. H., New York
  • Neidhardt, F.C., Bloch, P.L., Smith, D.F., (1974) J. Bacteriol., 119, pp. 736-747
  • Gesteland, R., Boedtker, H., (1964) J. Mol. Biol., 8, pp. 496-507
  • Kessler, S.W., (1975) J. Immunol., 115, pp. 1617-1624
  • Thomas, J.O., (1978) Techniques in protein and enzyme biochemistry, pp. 1-22. , B106, Elsevier/North Holland, New York
  • Fox, B.W., (1976) Techniques of sample preparation for liquid scintillation counting, , North Holland, Amsterdam
  • O'Farrell, P.H., (1975) J. Biol. Chem., 250, pp. 4007-4021
  • O'Farrell, P.Z., Goodman, H.M., O'Farrell, P.H., (1977) Cell, 12, pp. 1133-1142
  • Chamberlain, J.P., (1979) Anal. Biochem., 98, pp. 132-135
  • Haworth, C., Heathcote, J.G., An improved technique for the analysis of amino acids and related compounds on thin layers of cellulose Part I. Qualitative separation (1969) Journal of Chromatography A, 41, pp. 380-385
  • Smith, I., Rider, L.J., Lerner, R.P., (1967) J. Chromatogr., 26, pp. 449-455
  • Fiers, W., Contreras, R., Duerinck, F., Haegeman, G., Merregaert, J., Min Jou, W., Raeymakers, F., Van Montagu, M., (1975) Nature (Lond.), 256, pp. 273-278
  • Verbraeken, E., Fiers, W., (1972) FEBS Lett., 28, pp. 89-92
  • Gorini, L., (1974) Ribosomes, , Nomura, M., Tissieres, A., Lengyel, P., eds, Cold Spring Harbor Laboratory, C. S. H., New York
  • Gorini, L., (1967) Fed. Proc., 26, p. 5
  • Stringini, P., Brickman, E., (1973) J. Mol. Biol., 75, pp. 659-672
  • Gorini, L., (1973) Proc. Natl Acad. Sci. USA, 70, pp. 2762-2766
  • Edelmann, P., Gallant, J., (1977) Cell, 10, pp. 131-137
  • Edelmann, P., Gallant, J., (1977) Proc. Natl Acad. Sci. USA, 74, pp. 3396-3398
  • Gorini, L., (1971) Nat. New Biol., 234, pp. 261-264
  • Funatsu, G., Nierhaus, K., Wittmann, H.G., (1972) Biochim. Biophys. Acta, 287, pp. 282-291
  • Parker, J., Johnston, T.C., Borgia, P.T., (1980) Mol. Gen. Genet., 180, pp. 275-281
  • Abraham, A.K., Pihl, A., (1980) Eur. J. Biochem., 106, pp. 257-262
  • Patterson, I., Kurland, C.G., (1980) Proc. Natl Acad. Sci. USA, 77, pp. 4007-4010
  • Wagner, G.H., Jelenc, P.C., Ehremberg, M., Kurland, C.G., (1982) Eur. J. Biochem., 122, pp. 193-197
  • Echandi, G., Algranati, I.D., (1975) Biochem. Biophys. Res. Commun., 67, pp. 1185-1191
  • Loftfield, R.B., Vanderjagt, D., (1972) Biochem. J., 128, pp. 1353-1356
  • Bouadloun, F., Donner, D., Kurland, C.G., (1983) EMBO J., 2, pp. 1351-1356
  • Rice, J.B., Libby, R.T., Reeve, J.N., (1984) J. Biol. Chem., 259, pp. 6505-6510
  • Yarus, M., (1979) Prog. Nucleic Acid Res., 23, pp. 195-225

Citas:

---------- APA ----------
McMURRY, L.M. & ALGRANATI, I.D. (1986) . Effect of polyamines on translation fidelity in vivo. European Journal of Biochemistry, 155(2), 383-390.
http://dx.doi.org/10.1111/j.1432-1033.1986.tb09502.x
---------- CHICAGO ----------
McMURRY, L.M., ALGRANATI, I.D. "Effect of polyamines on translation fidelity in vivo" . European Journal of Biochemistry 155, no. 2 (1986) : 383-390.
http://dx.doi.org/10.1111/j.1432-1033.1986.tb09502.x
---------- MLA ----------
McMURRY, L.M., ALGRANATI, I.D. "Effect of polyamines on translation fidelity in vivo" . European Journal of Biochemistry, vol. 155, no. 2, 1986, pp. 383-390.
http://dx.doi.org/10.1111/j.1432-1033.1986.tb09502.x
---------- VANCOUVER ----------
McMURRY, L.M., ALGRANATI, I.D. Effect of polyamines on translation fidelity in vivo. Eur. J. Biochem. 1986;155(2):383-390.
http://dx.doi.org/10.1111/j.1432-1033.1986.tb09502.x